The identification of MARCKS protein dates back to 1982 when it was found that an 87 kDa acidic protein in rat brain nerve endings could be regulated by calcium and calmodulin through the activation of PKC (Wu, W. C. et al. (1982) Proc. Natl. Acad. Sci. USA 79(17):5249-5253). Subsequently, the protein was officially named myristoylated alanine-rich C kinase substrate (MARCKS or MARKS) (Albert, K. A. et al. (1986) Proc. Natl. Acad. Sci. USA 83(9):2822-2826). MARCKS is ubiquitously expressed in various species and tissues (Albert, K. A. et al. (1987) Proc. Natl. Acad. Sci. USA 84(20):7046-7050; Stumpo, D. J. et al. (1989) Proc. Natl. Acad. Sci. USA 86(11):4012-4016), while the other MARCKS family member, MARCKS-related protein (MRP, also known as MacMARCKS, F52 or MLP), a 20 kDa protein is highly expressed in brain, reproductive tissues and macrophage (Aderem, A. (1992) Trend. Biochem. Sci. 17(10):438-443; Blacksher, P. J. (1993) J. Biol. Chem. 268:1501-1504). MRP, similar to MARCKS also contains the same three evolutionarily conserved domains; N-terminus myristoylation domain, multiple homology 2 (MH2) domain, and the effector domain (ED). The MH2 domain of unknown function resembles the cytoplasmic tail of the cation-independent mannose-6-phosphate receptor. Protein phosphorylation occurs at Ser159/163 of ED domain. The corporation between the N-terminus (myristoylated) and the ED (phosphorylated or not phosphorylated) is essential for controlling the association of these molecules with membranes.